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Purification and Characteristics of Serine Protease from the Head of Pacific White Shrimp
Yanyan Wu,Ping Wang,Laihao Li,Xianqing Yang,Shiqiang Diao 한국식품과학회 2012 Food Science and Biotechnology Vol.21 No.4
Serine protease from the head of Pacific white shrimp was purified by the following techniques: ammonium sulfate fractionation, Q-Sepharose HP ion exchange chromatography, and Sephadex G-100 gel filtration. The molecular weight was estimated as 32.8 kDa using SDSPAGE. The optimum pH and temperature of the enzyme for the hydrolysis of casein were determined to be 10.0 and 40oC. It was stable at pH range from 8.0 to 11.0 and had good thermal stability. Pb2+, Ca2+, Mg2+, Cu2+, and Mn2+could active the enzyme certainly when Zn2+and Hg2+strongly inhibited the activity. The enzyme was inhibited by the general serine protease inhibitor (PMSF) and the specific trypsin inhibitors (TLCK, SBTI). The modification of various amino acid modifiers for the purified enzyme determined that the enzyme active center included tryptophan,histidine, and serine, moreover, arginine had a certain relationship with the enzyme activity.